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PUBMED FOR HANDHELDS

Journal Abstract Search


226 related items for PubMed ID: 15890921

  • 1. Identification of residues in the hepatitis C virus core protein that are critical for capsid assembly in a cell-free system.
    Klein KC, Dellos SR, Lingappa JR.
    J Virol; 2005 Jun; 79(11):6814-26. PubMed ID: 15890921
    [Abstract] [Full Text] [Related]

  • 2. Unique features of hepatitis C virus capsid formation revealed by de novo cell-free assembly.
    Klein KC, Polyak SJ, Lingappa JR.
    J Virol; 2004 Sep; 78(17):9257-69. PubMed ID: 15308720
    [Abstract] [Full Text] [Related]

  • 3. Core protein domains involved in hepatitis C virus-like particle assembly and budding at the endoplasmic reticulum membrane.
    Hourioux C, Ait-Goughoulte M, Patient R, Fouquenet D, Arcanger-Doudet F, Brand D, Martin A, Roingeard P.
    Cell Microbiol; 2007 Apr; 9(4):1014-27. PubMed ID: 17257269
    [Abstract] [Full Text] [Related]

  • 4. Alanine scanning of the hepatitis C virus core protein reveals numerous residues essential for production of infectious virus.
    Murray CL, Jones CT, Tassello J, Rice CM.
    J Virol; 2007 Oct; 81(19):10220-31. PubMed ID: 17634240
    [Abstract] [Full Text] [Related]

  • 5. The Replacement of 10 Non-Conserved Residues in the Core Protein of JFH-1 Hepatitis C Virus Improves Its Assembly and Secretion.
    Etienne L, Blanchard E, Boyer A, Desvignes V, Gaillard J, Meunier JC, Roingeard P, Hourioux C.
    PLoS One; 2015 Oct; 10(9):e0137182. PubMed ID: 26339783
    [Abstract] [Full Text] [Related]

  • 6. Cell-Free Hepatitis B Virus Capsid Assembly Dependent on the Core Protein C-Terminal Domain and Regulated by Phosphorylation.
    Ludgate L, Liu K, Luckenbaugh L, Streck N, Eng S, Voitenleitner C, Delaney WE, Hu J.
    J Virol; 2016 Jun 15; 90(12):5830-5844. PubMed ID: 27076641
    [Abstract] [Full Text] [Related]

  • 7. Identification of basic amino acids at the N-terminal end of the core protein that are crucial for hepatitis C virus infectivity.
    Alsaleh K, Delavalle PY, Pillez A, Duverlie G, Descamps V, Rouillé Y, Dubuisson J, Wychowski C.
    J Virol; 2010 Dec 15; 84(24):12515-28. PubMed ID: 20943968
    [Abstract] [Full Text] [Related]

  • 8. Hepatitis C virus-like particle budding: role of the core protein and importance of its Asp111.
    Blanchard E, Hourioux C, Brand D, Ait-Goughoulte M, Moreau A, Trassard S, Sizaret PY, Dubois F, Roingeard P.
    J Virol; 2003 Sep 15; 77(18):10131-8. PubMed ID: 12941925
    [Abstract] [Full Text] [Related]

  • 9. Signal peptide peptidase-catalyzed cleavage of hepatitis C virus core protein is dispensable for virus budding but destabilizes the viral capsid.
    Vauloup-Fellous C, Pène V, Garaud-Aunis J, Harper F, Bardin S, Suire Y, Pichard E, Schmitt A, Sogni P, Pierron G, Briand P, Rosenberg AR.
    J Biol Chem; 2006 Sep 22; 281(38):27679-92. PubMed ID: 16849324
    [Abstract] [Full Text] [Related]

  • 10. Dimerization of rubella virus capsid protein is not required for virus particle formation.
    Lee JY, Hwang D, Gillam S.
    Virology; 1996 Feb 01; 216(1):223-7. PubMed ID: 8614992
    [Abstract] [Full Text] [Related]

  • 11. Identification of hepatitis B virus core protein residues critical for capsid assembly, pgRNA encapsidation and resistance to capsid assembly modulators.
    Luo Y, Cheng J, Hu Z, Ban H, Wu S, Hwang N, Kulp J, Li Y, Du Y, Chang J, Viswanathan U, Guo JT.
    Antiviral Res; 2021 Jul 01; 191():105080. PubMed ID: 33933516
    [Abstract] [Full Text] [Related]

  • 12. Genetic analysis of the carboxy-terminal region of the hepatitis C virus core protein.
    Kopp M, Murray CL, Jones CT, Rice CM.
    J Virol; 2010 Feb 01; 84(4):1666-73. PubMed ID: 20007277
    [Abstract] [Full Text] [Related]

  • 13. The hydrophilic amino-terminal arm of reovirus core shell protein lambda1 is dispensable for particle assembly.
    Kim J, Zhang X, Centonze VE, Bowman VD, Noble S, Baker TS, Nibert ML.
    J Virol; 2002 Dec 01; 76(23):12211-22. PubMed ID: 12414960
    [Abstract] [Full Text] [Related]

  • 14. Specific in vitro association between the hepatitis C viral genome and core protein.
    Fan Z, Yang QR, Twu JS, Sherker AH.
    J Med Virol; 1999 Oct 01; 59(2):131-4. PubMed ID: 10459145
    [Abstract] [Full Text] [Related]

  • 15. Proline residues in the HIV-1 NH2-terminal capsid domain: structure determinants for proper core assembly and subsequent steps of early replication.
    Fitzon T, Leschonsky B, Bieler K, Paulus C, Schröder J, Wolf H, Wagner R.
    Virology; 2000 Mar 15; 268(2):294-307. PubMed ID: 10704338
    [Abstract] [Full Text] [Related]

  • 16. Mutations in the STAT1‑interacting domain of the hepatitis C virus core protein modulate the response to antiviral therapy.
    Anjum S, Afzal MS, Ahmad T, Aslam B, Waheed Y, Shafi T, Qadri I.
    Mol Med Rep; 2013 Aug 15; 8(2):487-92. PubMed ID: 23799612
    [Abstract] [Full Text] [Related]

  • 17. Self-assembly of nucleocapsid-like particles from recombinant hepatitis C virus core protein.
    Kunkel M, Lorinczi M, Rijnbrand R, Lemon SM, Watowich SJ.
    J Virol; 2001 Mar 15; 75(5):2119-29. PubMed ID: 11160716
    [Abstract] [Full Text] [Related]

  • 18. Oligomerization of hepatitis C virus core protein is crucial for interaction with the cytoplasmic domain of E1 envelope protein.
    Nakai K, Okamoto T, Kimura-Someya T, Ishii K, Lim CK, Tani H, Matsuo E, Abe T, Mori Y, Suzuki T, Miyamura T, Nunberg JH, Moriishi K, Matsuura Y.
    J Virol; 2006 Nov 15; 80(22):11265-73. PubMed ID: 16971440
    [Abstract] [Full Text] [Related]

  • 19. A method for in vitro assembly of hepatitis C virus core protein and for screening of inhibitors.
    Fromentin R, Majeau N, Laliberté Gagné ME, Boivin A, Duvignaud JB, Leclerc D.
    Anal Biochem; 2007 Jul 01; 366(1):37-45. PubMed ID: 17493576
    [Abstract] [Full Text] [Related]

  • 20. hepatitis c Virus p7 is critical for capsid assembly and envelopment.
    Gentzsch J, Brohm C, Steinmann E, Friesland M, Menzel N, Vieyres G, Perin PM, Frentzen A, Kaderali L, Pietschmann T.
    PLoS Pathog; 2013 Jul 01; 9(5):e1003355. PubMed ID: 23658526
    [Abstract] [Full Text] [Related]


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